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Korean J Parasitol > Volume 5(3):1967 > Article

Original Article
Korean J Parasitol. 1967 Dec;5(3):125-133. English.
Published online Mar 20, 1994.  http://dx.doi.org/10.3347/kjp.1967.5.3.125
Copyright © 1967 by The Korean Society for Parasitology
Studies on malic dehydrogenase activity in parasitic helminths
Eun Hee Lee and Byong Seol Seo
Department of Parasitology and Institute of Endemic diseases, College of Medicine, Seoul National University, Korea.
Abstract

The malic dehydrogenase activity was determined by the modified method of Ochoa (1955) using tissue homogenates of various parasitic helminths.

Worm parasites were mostly collected from local abattoir, and removed from the organ or tissues of the naturally infected animal hosts, and some materials were also obtained from the human hosts. The helminths used in this experiment include 3 kinds of nematodes, 5 kinds of trematodes, and 8 kinds of cestodes.

They were throughly washed and homogenized in glass tissue grinder in ice chilled water bath, and then centrifuged. The supernatants were designated as enzyme preparations. The hydrogen concentrations of buffer solution were pH 1.4, 2.7, 3.5, 4.2, 5.2, 7.4, 8.2, 9.3, 10.2, 11.6, and enzymatic reaction of this experiment was performed at incubation temperature of 20, 30, 40, and 50℃. The extinction of Nicotinamide Adenosine Dinucleotide (NAD) was measured by spectrophotometry at the wave length of 340 millimicron.

The results of the experiment were as follows:

1. The malic dehydrogenase activity occurred over all kinds of parasitic helminths used in this study. And the activity on sparganum turned out to be highest.

2. All helminths displayed their maximum activity in the range of alkaline pH.

3. A comparison of the effects of temperature and substrate concentration on the enzyme activity was made among these helminths. However, no definite relationship among them has been detected.

4. The significance of the existence of this enzyme in the helminths was briefly discussed.

Figures


Fig. 1
MDH activity in 3 kinds of nematodes.


Fig. 2
MDH activity in 5 kinds of trematodes.


Fig. 3
MDH activity in 4 kinds of cestodes.


Fig. 4
MDH activity in Taenia solinm.


Fig. 5
MDH activity in Teania pisiformis.


Fig. 6
Relation between MDH activity and incubation temperature in nematodes.


Fig. 7
Relation between MDH activity and incubation temperature in trematodes.


Fig. 8
Relation between MDH activity and incubation temperature in cestodes (Cyclophyllidea).


Fig. 9
Relation between MDH activity and incubation temperature in larval and adult cestodes (Pseudophyllidea).


Fig. 10
Effects of the substrate concentration on the MDH activity in nematodes.


Fig. 11
Effects of the substrate concentration on the MDH activity in trematodes.


Fig. 12
Effects of the substrate concentration on the MDH activity in cestodes.

Tables


Table 1
Malic Dehydrogenase Activities in Various Parasitic Helminths (Changes in Optical Density per milligram nitrogen of worm tissue)


Table 2
Malic dehydrogenase activities in parasitic hilminths by the variation of incubation temperature. (Changes in O.D./mgN/min. of worm tissues)


Table 3
Malic dehydrogenase activities in parasitic hilminths by the variation of substrate concentration. (Changes in O.D./mgN/min. of worm tissue)

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